MoLuc Protein-Protein Interaction System
Signosis' MoLuc™ Protein–Protein Interaction (PPI) System is a newly engineered split luciferase reporter platform for the sensitive detection of intracellular protein–protein interactions (PPIs). The two MoLuc™ luciferase subunits are fused to proteins of interest. When the target proteins interact, the two luciferase fragments are brought into close proximity, reconstituting an active enzyme that generates a bright luminescent signal for rapid and quantitative detection of PPIs in living cells.
In addition to our ready-to-use MoLuc™ PPI reagents, Signosis offers custom protein pair services, enabling researchers to generate tailored MoLuc™ fusion constructs and cell-based assays for virtually any protein interaction of interest. Our custom solutions support target validation, mechanism-of-action studies, and drug screening for both academic and pharmaceutical research.
Advantages of the Signosis MoLuc™ Protein–Protein Interaction (PPI) System
The Signosis MoLuc™ Protein–Protein Interaction (PPI) System is designed to provide a sensitive, flexible, and user-friendly platform for studying protein interactions in living cells.
Patent-free platform
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Developed as a patent-free alternative, providing researchers and commercial partners with greater flexibility while avoiding dependence on proprietary split-luciferase technologies.
Flexible fusion design
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Compatible with N- or C-terminal fusion of target proteins, allowing optimization for a wide variety of protein pairs.
High sensitivity
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Engineered to generate a robust luminescent signal with a high signal-to-background ratio, enabling detection of weak or transient protein interactions.
Low background luminescence
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Optimized luciferase fragment design minimizes spontaneous complementation, improving assay specificity.
Rapid and quantitative readout
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Produces a luminescent signal that can be measured using standard luminometers without specialized instrumentation.
Cost-effective solution
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Designed to provide a competitive alternative for laboratories seeking reliable PPI assays with reduced overall assay costs.
PPI Positive Control Pair
The FKBP–FRB protein pair is available separately as an inducible positive control for validating MoLuc™ protein–protein interaction assays. Upon the addition of rapamycin, FKBP and FRB rapidly dimerize, bringing the two MoLuc™ fragments into close proximity and generating a robust luminescent signal.
Name | SKU | Formatted Price |
|---|---|---|
PPI Positive Control Pair (FKBP-FRB) | PPI-0001 | $620.00 |
GPCR-β-Arrestin 2 Interactions
Upon activation by an agonist, many GPCRs recruit β-arrestin 2, a key adaptor protein that mediates receptor desensitization, internalization, and β-arrestin-dependent signaling pathways.
The Signosis MoLuc™ GPCR–β-Arrestin 2 Interaction System enables sensitive detection of GPCR–β-arrestin 2 interactions in cells using the proprietary MoLuc™ split luciferase technology. By fusing the two MoLuc™ fragments to a GPCR and β-arrestin 2, receptor activation induces protein–protein interaction, reconstituting an active luciferase enzyme that generates a bright luminescent signal.
This cell-based assay provides a rapid, quantitative, and highly sensitive platform for identifying biased agonists and screening compounds that modulate GPCR signaling.
Signosis also offers custom GPCR–β-arrestin 2 assay development services, enabling researchers to generate tailored assays for virtually any GPCR target to support target validation, mechanism-of-action studies, and drug discovery.
Name | SKU | Formatted Price |
|---|---|---|
MoLuc GLP1R–β-Arrestin 2 Interaction System | PPI-0002 | $1,160.00 |